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P22534

- GUNA_CALSA

UniProt

P22534 - GUNA_CALSA

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Protein

Endoglucanase A

Gene
celA
Organism
Caldicellulosiruptor saccharolyticus (Caldocellum saccharolyticum)
Status
Reviewed - Annotation score: 4 out of 5 - Protein inferred from homologyi

Functioni

The N-terminal domain of CelA codes for an endoglucanase activity on carboxymethylcellulose. The C-terminal domain probably acts synergistically to hydrolyze crystalline cellulose.

Catalytic activityi

Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei396 – 3961 By similarity
Active sitei434 – 4341 By similarity
Active sitei443 – 4431 By similarity

GO - Molecular functioni

  1. cellulase activity Source: UniProtKB-EC
  2. cellulose binding Source: InterPro

GO - Biological processi

  1. cellulose catabolic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Cellulose degradation, Polysaccharide degradation

Protein family/group databases

CAZyiCBM3. Carbohydrate-Binding Module Family 3.
GH48. Glycoside Hydrolase Family 48.
GH9. Glycoside Hydrolase Family 9.

Names & Taxonomyi

Protein namesi
Recommended name:
Endoglucanase A (EC:3.2.1.4)
Alternative name(s):
Cellulase A
Endo-1,4-beta-glucanase A
Gene namesi
Name:celA
OrganismiCaldicellulosiruptor saccharolyticus (Caldocellum saccharolyticum)
Taxonomic identifieri44001 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaThermoanaerobacteralesThermoanaerobacterales Family III. Incertae SedisCaldicellulosiruptor

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2323 Reviewed predictionAdd
BLAST
Chaini24 – 17421719Endoglucanase APRO_0000007944Add
BLAST

Post-translational modificationi

The linker region (also termed "hinge") may be a potential site for proteolysis.

Structurei

3D structure databases

ProteinModelPortaliP22534.
SMRiP22534. Positions 26-636, 1117-1739.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini477 – 637161CBM3 1Add
BLAST
Domaini703 – 856154CBM3 2Add
BLAST
Domaini906 – 1059154CBM3 3Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni24 – 476453Catalytic 1Add
BLAST
Regioni638 – 70265Linker ("hinge") (Pro-Thr box)Add
BLAST
Regioni857 – 90549Linker ("hinge") (Pro-Thr box)Add
BLAST
Regioni1060 – 111253Linker ("hinge") (Pro-Thr box)Add
BLAST
Regioni1113 – 1742630Catalytic 2Add
BLAST

Sequence similaritiesi

In the N-terminal section; belongs to the glycosyl hydrolase 9 (cellulase E) family.
In the C-terminal section; belongs to the glycosyl hydrolase 48 (cellulase L) family.

Keywords - Domaini

Repeat, Signal

Family and domain databases

Gene3Di1.50.10.10. 5 hits.
2.60.40.710. 3 hits.
4.10.870.10. 1 hit.
InterProiIPR008928. 6-hairpin_glycosidase-like.
IPR012341. 6hp_glycosidase.
IPR008965. Carb-bd_dom.
IPR001956. CBD_3.
IPR027390. Endoglucanase_F_dom3.
IPR000556. Glyco_hydro_48F.
IPR001701. Glyco_hydro_9.
IPR018221. Glyco_hydro_9_AS.
[Graphical view]
PfamiPF00942. CBM_3. 3 hits.
PF02011. Glyco_hydro_48. 1 hit.
PF00759. Glyco_hydro_9. 1 hit.
[Graphical view]
PRINTSiPR00844. GLHYDRLASE48.
SMARTiSM01067. CBM_3. 3 hits.
[Graphical view]
SUPFAMiSSF48208. SSF48208. 2 hits.
SSF49384. SSF49384. 3 hits.
PROSITEiPS51172. CBM3. 3 hits.
PS00592. GLYCOSYL_HYDROL_F9_1. 1 hit.
PS00698. GLYCOSYL_HYDROL_F9_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P22534-1 [UniParc]FASTAAdd to Basket

« Hide

MVVTFLFILG VVYGVKPWQE ARAGSFNYGE ALQKAIMFYE FQMSGKLPNW     50
VRNNWRGDSA LKDGQDNGLD LTGGWFDAGD HVKFNLPMSY TGTMLSWAAY 100
EYKDAFVKSG QLEHILNQIE WVNDYFVKCH PSKYVYYYQV GDGGKDHAWW 150
GPAEVMQMER PSFKVTQSSP GSAVVAETAA SLAAASIVLK DRNPTKAATY 200
LQHAKDLYEF AEVTKSDSGY TAANGYYNSW SGFYDELSWA AVWLYLATND 250
STYLTKAESY VQNWPKISGS NIIDYKWAHC WDDVHNGAAL LLAKITDKDT 300
YKQIIESHLD YWTTGYNGER IKYTPKGLAW LDQWGSLRYA TTTAFLAFVY 350
SDWSGCPTGK KETYRKFGES QIDYALGSTG RSFVVGFGTN PPKRPHHRTA 400
HSSWADSQSI PSYHRHTLYG ALVGGPGSDD SYTDDISNYV NNEVACDYNA 450
GFVGALAKMY LLYGGNPIPD FKAIETPTND EFFVEAGINA SGTNFIEIKA 500
IVNNQSGWPA RATNKLKFRY FVDLSELIKA GYSPNQLTLS TNYNQGAKVS 550
GPYVWDSSRN IYYILVDFTG TLIYPGGQDK YKKEVQFRIA APQNVQWDNS 600
NDYSFQDIKG VSSGSVVKTK YIPLYDEDIK VWGEEPGTSG VSPTPTASVT 650
PTPTPTPTAT PTPTPTPTVT PTPTVTATPT PTPTPTSTPT VTPTPTPVST 700
PATSGQIKVL YANKETNSTT NTIRPWLKVV NSGSSSIDLS RVTIRYWYTV 750
DGERAQSAIS DWAQIGASNV TFKFVKLSSS VSGADYYLEI GFKSGAGQLQ 800
PGKDTGEIQI RFNKDDWSNY NQGNDWSWIQ SMTSYGENEK VTAYIDGVLV 850
WGQEPSGTTP APTSTPTVTV TPTPTPTPTV TPTPTVTATP TPTPTPTSTP 900
VSTPATGGQI KVLYANKETN STTNTIRPWL KVVNSGSSSI DLSRVTIRYW 950
YTVDGERAQS AISDWAQIGA SNVTFKFVKL SSSVSGADYY LEIGFKSGAG 1000
QLQPGKDTGE IQIRFNKDDW SNYNQGNDWS WIQSMTSYGE NEKVTAYIDG 1050
VLVWGQEPSG ATPAPTVTPT PTVTPTPTPA PTPTATPTPT PTPTVTPTPT 1100
VAPTPTPSST PSGLGKYGQR FMWLWNKIHD PASGYFNQDG IPYHSVETLI 1150
CEAPDYGHLT TSEAFSYYVW LEAVYGKLTG DWSKFKTAWD TLEKYMIPSA 1200
EDQPMRSYDP NKPATYAGEW ETPDKYPSPL EFNVPVGKDP LHNELVSTYG 1250
STLMYGMHWL MDVDNWYGYG KRGDGVSRAS FINTFQRGPE ESVWETVPHP 1300
SWEEFKWGGP NGFLDLFIKD QNYSKQWRYT NAPDADARAI QATYWAKVWA 1350
KEQGKFNEIS SYVGKAAKMG DYLRYAMFDK YFKPLGCQDK NAAGGTGYDS 1400
AHYLLSWYYA WGGALDGAWS WKIGCSHAHF GYQNPMAAWA LANDSDMKPK 1450
SPNGASDWAK SLKRQIEFYR WLQSAEGAIA GGATNSWNGR YEKYPAGTAT 1500
FYGMAYEPNP VYRDPGSNTW FGFQAWSMQR VAEYYYVTGD KDAGTLLEKW 1550
VSWIKSVVKL NSDGTFAIPS TLDWSGQPDT WNGTYTGNPN LHVKVVDYGT 1600
DLGITASLAN ALLYYSAGTK KYGVFDEEAK NLAKELLDRM WKLYRDEKGL 1650
SAPEKRADYK RFFEQEVYIP AGWTGKMPNG DVIKSGVKFI DIRSKYKQDP 1700
DWPKLEAAYK SGQVPEFRYH RFWAQCDIAI VNATYEILFG NQ 1742
Length:1,742
Mass (Da):193,697
Last modified:October 1, 1996 - v2
Checksum:i3F0699A2123EED07
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1545 – 15451T → A in AAA72860. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L32742 Genomic DNA. Translation: AAA91086.1.
M36063 Genomic DNA. Translation: AAA72860.1.
L01257 Unassigned DNA. No translation available.
PIRiT17120.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L32742 Genomic DNA. Translation: AAA91086.1 .
M36063 Genomic DNA. Translation: AAA72860.1 .
L01257 Unassigned DNA. No translation available.
PIRi T17120.

3D structure databases

ProteinModelPortali P22534.
SMRi P22534. Positions 26-636, 1117-1739.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

CAZyi CBM3. Carbohydrate-Binding Module Family 3.
GH48. Glycoside Hydrolase Family 48.
GH9. Glycoside Hydrolase Family 9.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Family and domain databases

Gene3Di 1.50.10.10. 5 hits.
2.60.40.710. 3 hits.
4.10.870.10. 1 hit.
InterProi IPR008928. 6-hairpin_glycosidase-like.
IPR012341. 6hp_glycosidase.
IPR008965. Carb-bd_dom.
IPR001956. CBD_3.
IPR027390. Endoglucanase_F_dom3.
IPR000556. Glyco_hydro_48F.
IPR001701. Glyco_hydro_9.
IPR018221. Glyco_hydro_9_AS.
[Graphical view ]
Pfami PF00942. CBM_3. 3 hits.
PF02011. Glyco_hydro_48. 1 hit.
PF00759. Glyco_hydro_9. 1 hit.
[Graphical view ]
PRINTSi PR00844. GLHYDRLASE48.
SMARTi SM01067. CBM_3. 3 hits.
[Graphical view ]
SUPFAMi SSF48208. SSF48208. 2 hits.
SSF49384. SSF49384. 3 hits.
PROSITEi PS51172. CBM3. 3 hits.
PS00592. GLYCOSYL_HYDROL_F9_1. 1 hit.
PS00698. GLYCOSYL_HYDROL_F9_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "celA, another gene coding for a multidomain cellulase from the extreme thermophile Caldocellum saccharolyticum."
    Te'O V.S. Jr., Saul D.J., Bergquist P.L.
    Appl. Microbiol. Biotechnol. 43:291-296(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Cloning, sequence analysis, and expression in Escherichia coli of a gene coding for a beta-mannanase from the extremely thermophilic bacterium 'Caldocellum saccharolyticum'."
    Luethi E., Jasmat N.B., Grayling R.A., Love D.R., Bergquist P.L.
    Appl. Environ. Microbiol. 57:694-700(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1516-1742.

Entry informationi

Entry nameiGUNA_CALSA
AccessioniPrimary (citable) accession number: P22534
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: October 1, 1996
Last modified: December 11, 2013
This is version 90 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi